Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
Structure of an RNase-related protein from Calystegia sepium.,Rabijns A, Verboven C, Rouge P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):627-33. Epub 2002, Mar 22. PMID:11914487[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rabijns A, Verboven C, Rouge P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ. Structure of an RNase-related protein from Calystegia sepium. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):627-33. Epub 2002, Mar 22. PMID:11914487
